Related Experiment Video
Updated: Jun 6, 2026

Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus
Published on: June 2, 2023
Protease purified from Schizophyllum commune culture broth digests fibrins without activating plasminogen
Chung-Lun Lu1, Jeng-Pang Wang, Shiu-Nan Chen
1Institute of Fisheries Science, National Taiwan University, Taipei, Taiwan.
Abstract:
Schizophyllum commune is a widely distributed mushroom used as an herbal medicine and an ingredient in healthy food. In this study, a protease from a fermented culture broth of S. commune demonstrated strong fibrinolytic and fibrinogenolytic activities. This fibrinolytic protease showed a suppression effect in blood coagulation in co-incubation with rat citrated blood through thromboelastographic analysis. The protease suppressed aggregation of fibrin (ogen), but not the platelets, in clotting formation and significantly decreased the clot strength. We also found very little potency in this protease to activate plasminogen, thus it exhibits the potential for an ideal fibrinolytic candidate for therapeutic applications in the future.

